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The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum
Author(s) -
Humphreys Michelle J.,
Moon Richard P.,
Klinder Annette,
Fowler Sylvia D.,
Rupp Katharina,
Bur Daniel,
Ridley Robert G.,
Berry Colin
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01597-5
Subject(s) - plasmodium berghei , plasmodium falciparum , biology , parasite hosting , malaria , pepstatin , virology , microbiology and biotechnology , biochemistry , enzyme , immunology , protease , world wide web , computer science
The gene encoding an aspartic proteinase precursor (proplasmepsin) from the rodent malaria parasite Plasmodium berghei has been cloned. Recombinant P. berghei plasmepsin hydrolysed a synthetic peptide substrate and this cleavage was prevented by the general aspartic proteinase inhibitor, isovaleryl pepstatin and by Ro40‐4388, a lead compound for the inhibition of plasmepsins from the human malaria parasite Plasmodium falciparum . Southern blotting detected only one proplasmepsin gene in P. berghei . Two plasmepsins have previously been reported in P. falciparum . Here, we describe two further proplasmepsin genes from this species. The suitability of P. berghei as a model for the in vivo evaluation of plasmepsin inhibitors is discussed.